Journal of Cell Science 115, e2002-e2002 (2002)
Copyright © 2002 The Company of Biologists Limited
doi:
CK2: a different kind of kinase?
We tend to think of kinases as signalling molecules that are switched on in
response to specific stimuli and phosphorylate a discrete set of effectors
appropriate to the response required. But CK2 is different: the kinase is
constitutively active with or without its non-catalytic ß subunits, and
it has >300 cellular substrates. So what exactly is its role? In a
Commentary on p. 3873, Lorenzo
Pinna discusses the apparent paradox of constitutive CK2 activity as well as
evidence that it can in fact be regulated. CK2 can be considered as an
independent executor whose activity is essential for the signalling network
but is not normally adjustable. Recent work, however, indicates that CK2 is
part of a pathway that inhibits RNA polymerase III activity when genome
integrity is compromised. In this case, the ß subunits target CK2 to
TATA-binding protein but these interactions can be disrupted by DNA damage
signalling. A similar mechanism could operate in the Wnt pathway; indeed,
ß-subunit-dependent targeting/docking might be a fundamental aspect of
CK2 function.

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Related articles in JCS:
- Protein kinase CK2: a challenge to canons
- Lorenzo A. Pinna
JCS 2002 115: 3873-3878.
[Abstract]
[Full Text]